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| | <StructureSection load='2vhh' size='340' side='right'caption='[[2vhh]], [[Resolution|resolution]] 2.80Å' scene=''> | | <StructureSection load='2vhh' size='340' side='right'caption='[[2vhh]], [[Resolution|resolution]] 2.80Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2vhh]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Drome Drome]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VHH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2VHH FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2vhh]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VHH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2VHH FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2vhi|2vhi]]</div></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8Å</td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Beta-ureidopropionase Beta-ureidopropionase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.1.6 3.5.1.6] </span></td></tr>
| + | |
| | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2vhh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vhh OCA], [https://pdbe.org/2vhh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2vhh RCSB], [https://www.ebi.ac.uk/pdbsum/2vhh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2vhh ProSAT]</span></td></tr> | | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2vhh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vhh OCA], [https://pdbe.org/2vhh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2vhh RCSB], [https://www.ebi.ac.uk/pdbsum/2vhh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2vhh ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q9VI04_DROME Q9VI04_DROME] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Beta-ureidopropionase]] | + | [[Category: Drosophila melanogaster]] |
| - | [[Category: Drome]]
| + | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Andersen, B]] | + | [[Category: Andersen B]] |
| - | [[Category: Dobritzsch, D]] | + | [[Category: Dobritzsch D]] |
| - | [[Category: Lohkamp, B]] | + | [[Category: Lohkamp B]] |
| - | [[Category: Lundgren, S]] | + | [[Category: Lundgren S]] |
| - | [[Category: Piskur, J]] | + | [[Category: Piskur J]] |
| - | [[Category: Hydrolase]]
| + | |
| Structural highlights
Function
Q9VI04_DROME
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Beta-alanine synthase (betaAS) is the third enzyme in the reductive pyrimidine catabolic pathway, which is responsible for the breakdown of the nucleotide bases uracil and thymine in higher organisms. It catalyzes the hydrolysis of N-carbamyl-beta-alanine and N-carbamyl-beta-aminoisobutyrate to the corresponding beta-amino acids. betaASs are grouped into two phylogenetically unrelated subfamilies, a general eukaryote one and a fungal one. To reveal the molecular architecture and understand the catalytic mechanism of the general eukaryote betaAS subfamily, we determined the crystal structure of Drosophila melanogaster betaAS to 2.8 A resolution. It shows a homooctameric assembly of the enzyme in the shape of a left-handed helical turn, in which tightly packed dimeric units are related by 2-fold symmetry. Such an assembly would allow formation of higher oligomers by attachment of additional dimers on both ends. The subunit has a nitrilase-like fold and consists of a central beta-sandwich with a layer of alpha-helices packed against both sides. However, the core fold of the nitrilase superfamily enzymes is extended in D. melanogaster betaAS by addition of several secondary structure elements at the N-terminus. The active site can be accessed from the solvent by a narrow channel and contains the triad of catalytic residues (Cys, Glu, and Lys) conserved in nitrilase-like enzymes.
The crystal structure of beta-alanine synthase from Drosophila melanogaster reveals a homooctameric helical turn-like assembly.,Lundgren S, Lohkamp B, Andersen B, Piskur J, Dobritzsch D J Mol Biol. 2008 Apr 11;377(5):1544-59. Epub 2008 Feb 13. PMID:18336837[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Lundgren S, Lohkamp B, Andersen B, Piskur J, Dobritzsch D. The crystal structure of beta-alanine synthase from Drosophila melanogaster reveals a homooctameric helical turn-like assembly. J Mol Biol. 2008 Apr 11;377(5):1544-59. Epub 2008 Feb 13. PMID:18336837 doi:10.1016/j.jmb.2008.02.011
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